› 6fm5

X-ray diffraction
1.47Å resolution

Crystal structure of self-complemented CsuA/B major subunit from archaic chaperone-usher Csu pili of Acinetobacter baumannii

Released:
DOI: 10.2210/pdb6fm5/pdb
PDB entry 6fm5 coloured by chain, front view.
PDB entry 6fm5 coloured by chain, side view.
PDB entry 6fm5 coloured by chain, top view.
Source organism: Acinetobacter baumannii
Primary publication:
Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.
Pakharukova N, McKenna S, Tuittila M, Paavilainen S, Malmi H, Xu Y, Parilova O, Matthews S, Zavialov AV
J Biol Chem 293 17070-17080 (2018)
PMID: 30228191

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180522 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spore coat protein U domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 17.64 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q6XBY7 (Residues: 38-180, 26-39; Coverage: 100%)
Gene name: csuA/B

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21212
Unit cell:
a: 49.214Å b: 92.018Å c: 34.111Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.197 0.219
Expression system: Escherichia coli BL21

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Citations

2 review citations

Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).
Behzadi P. (2020)
1 more

2 mentions without citation

Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information.
Pakharukova et al. (2018)
1 more